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Showing Protein Enoyl-CoA hydratase, mitochondrial (HMDBP00388)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 31 metabolites
Identification
HMDB Protein ID HMDBP00388
Secondary Accession Numbers
  • 5625
  • HMDBP05421
Name Enoyl-CoA hydratase, mitochondrial
Synonyms
  1. Enoyl-CoA hydratase 1
  2. SCEH
  3. Short-chain enoyl-CoA hydratase
Gene Name ECHS1
Protein Type Enzyme
Biological Properties
General Function Involved in catalytic activity
Specific Function Straight-chain enoyl-CoA thioesters from C4 up to at least C16 are processed, although with decreasing catalytic rate.
Pathways
  • 2-aminoadipic 2-oxoadipic aciduria
  • 2-Methyl-3-Hydroxybutryl CoA Dehydrogenase Deficiency
  • 3-Hydroxy-3-Methylglutaryl-CoA Lyase Deficiency
  • 3-hydroxyisobutyric acid dehydrogenase deficiency
  • 3-hydroxyisobutyric aciduria
  • 3-Methylcrotonyl Coa Carboxylase Deficiency Type I
  • 3-Methylglutaconic Aciduria Type I
  • 3-Methylglutaconic Aciduria Type III
  • 3-Methylglutaconic Aciduria Type IV
  • beta-Alanine metabolism
  • Beta-Ketothiolase Deficiency
  • Butanoate metabolism
  • Butyrate Metabolism
  • Carnitine palmitoyl transferase deficiency (I)
  • Carnitine palmitoyl transferase deficiency (II)
  • Ethylmalonic Encephalopathy
  • fatty acid beta-oxidation
  • Fatty acid elongation
  • Fatty Acid Elongation In Mitochondria
  • Fatty acid Metabolism
  • fatty acid metabolism
  • Glutaric Aciduria Type I
  • Glutaric Aciduria Type I
  • Hyperlysinemia I, Familial
  • Hyperlysinemia II or Saccharopinuria
  • Isobutyryl-coa dehydrogenase deficiency
  • Isovaleric acidemia
  • Isovaleric Aciduria
  • Long chain acyl-CoA dehydrogenase deficiency (LCAD)
  • Long-chain-3-hydroxyacyl-coa dehydrogenase deficiency (LCHAD)
  • Lysine degradation
  • Lysine degradation
  • Malonic Aciduria
  • Malonyl-coa decarboxylase deficiency
  • Maple Syrup Urine Disease
  • Medium chain acyl-coa dehydrogenase deficiency (MCAD)
  • Methylmalonate Semialdehyde Dehydrogenase Deficiency
  • Methylmalonic Aciduria
  • Methylmalonic Aciduria Due to Cobalamin-Related Disorders
  • Mitochondrial Beta-Oxidation of Long Chain Saturated Fatty Acids
  • Mitochondrial Beta-Oxidation of Medium Chain Saturated Fatty Acids
  • Mitochondrial Beta-Oxidation of Short Chain Saturated Fatty Acids
  • Propanoate metabolism
  • Propanoate metabolism
  • Propionic Acidemia
  • Pyridoxine dependency with seizures
  • Saccharopinuria/Hyperlysinemia II
  • Short Chain Acyl CoA Dehydrogenase Deficiency (SCAD Deficiency)
  • Short-chain 3-hydroxyacyl-CoA dehydrogenase deficiency (SCHAD)
  • Trifunctional protein deficiency
  • Tryptophan metabolism
  • Valine, leucine and isoleucine degradation
  • Valine, leucine and isoleucine degradation
  • Very-long-chain acyl coa dehydrogenase deficiency (VLCAD)
Reactions
(3S)-3-hydroxyacyl-CoA → trans-2(or 3)-enoyl-CoA + Water details
(3S)-3-Hydroxyacyl-CoA → trans-2,3-Dehydroacyl-CoA + Water details
3-Hydroxybutyryl-CoA → Crotonoyl-CoA + Water details
3-Hydroxypropionyl-CoA → Acrylyl-CoA + Water details
3-Hydroxyisovaleryl-CoA → 3-Methylcrotonyl-CoA + Water details
(S)-3-Hydroxydodecanoyl-CoA → (2E)-Dodecenoyl-CoA + Water details
2-Methyl-3-hydroxybutyryl-CoA → Tiglyl-CoA + Water details
Methacrylyl-CoA + Water → (S)-3-Hydroxyisobutyryl-CoA details
(S)-3-Hydroxyhexadecanoyl-CoA → (2E)-Hexadecenoyl-CoA + Water details
(S)-3-Hydroxytetradecanoyl-CoA → (2E)-Tetradecenoyl-CoA + Water details
(S)-Hydroxydecanoyl-CoA → (2E)-Decenoyl-CoA + Water details
(S)-Hydroxyoctanoyl-CoA → (2E)-Octenoyl-CoA + Water details
(S)-Hydroxyhexanoyl-CoA → trans-2-Hexenoyl-CoA + Water details
Crotonoyl-CoA + Water → 3-Hydroxybutyryl-CoA details
5-Carboxy-2-pentenoyl-CoA + Water → (3S)-3-Hydroxyadipyl-CoA details
GO Classification
Biological Process
fatty acid beta-oxidation
Cellular Component
mitochondrial matrix
Function
catalytic activity
Molecular Function
enoyl-CoA hydratase activity
Process
metabolic process
Cellular Location
  1. Mitochondrion matrix
Gene Properties
Chromosome Location 10
Locus 10q26.2-q26.3
SNPs ECHS1
Gene Sequence 
>873 bp
ATGGCCGCCCTGCGTGTCCTGCTGTCCTGCGTCCGCGGCCCGCTGAGGCCCCCGGTTCGC
TGTCCCGCCTGGCGTCCCTTCGCCTCGGGTGCTAACTTTGAGTACATCATCGCAGAAAAA
AGAGGGAAGAATAACACCGTGGGGTTGATCCAACTGAACCGCCCCAAGGCCCTCAATGCA
CTTTGCGATGGCCTGATTGACGAGCTCAACCAGGCCCTGAAGACCTTCGAGGAGGACCCG
GCCGTGGGGGCCATTGTCCTCACCGGCGGGGATAAGGCCTTTGCAGCTGGAGCTGATATC
AAGGAAATGCAGAACCTGAGTTTCCAGGACTGTTACTCCAGCAAGTTCTTGAAGCACTGG
GACCACCTCACCCAGGTCAAGAAGCCAGTCATCGCTGCTGTCAATGGCTATGCCTTTGGC
GGGGGCTGTGAGCTTGCCATGATGTGTGATATCATCTATGCCGGTGAGAAGGCCCAGTTT
GCACAGCCGGAGATCTTAATAGGAACCATCCCAGGTGCGGGCGGCACCCAGAGACTCACC
CGTGCTGTTGGGAAGTCGCTGGCGATGGAGATGGTCCTCACTGGTGACCGGATCTCAGCC
CAGGACGCCAAGCAAGCAGGTCTTGTCAGCAAGATTTGTCCTGTTGAGACACTGGTGGAA
GAAGCCATCCAGTGTGCAGAAAAAATTGCCAGCAATTCTAAAATTGTAGTAGCGATGGCC
AAAGAATCAGTGAATGCAGCTTTTGAAATGACATTAACAGAAGGAAGTAAGTTGGAGAAG
AAACTCTTTTATTCAACCTTTGCCACTGATGACCGGAAAGAAGGGATGACCGCGTTTGTG
GAAAAGAGAAAGGCCAACTTCAAAGACCAGTGA
Protein Properties
Number of Residues 290
Molecular Weight 31387.085
Theoretical pI 8.073
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>Enoyl-CoA hydratase, mitochondrial
MAALRVLLSCVRGPLRPPVRCPAWRPFASGANFEYIIAEKRGKNNTVGLIQLNRPKALNA
LCDGLIDELNQALKTFEEDPAVGAIVLTGGDKAFAAGADIKEMQNLSFQDCYSSKFLKHW
DHLTQVKKPVIAAVNGYAFGGGCELAMMCDIIYAGEKAQFAQPEILIGTIPGAGGTQRLT
RAVGKSLAMEMVLTGDRISAQDAKQAGLVSKICPVETLVEEAIQCAEKIASNSKIVVAMA
KESVNAAFEMTLTEGSKLEKKLFYSTFATDDRKEGMTAFVEKRKANFKDQ
GenBank ID Protein 55664849
UniProtKB/Swiss-Prot ID P30084
UniProtKB/Swiss-Prot Entry Name ECHM_HUMAN
PDB IDs
GenBank Gene ID AL360181
GeneCard ID ECHS1
GenAtlas ID ECHS1
HGNC ID HGNC:3151
References
General References
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  2. Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [PubMed:1286669 ]
  3. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
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  5. Kanazawa M, Ohtake A, Abe H, Yamamoto S, Satoh Y, Takayanagi M, Niimi H, Mori M, Hashimoto T: Molecular cloning and sequence analysis of the cDNA for human mitochondrial short-chain enoyl-CoA hydratase. Enzyme Protein. 1993;47(1):9-13. [PubMed:8012501 ]
  6. Janssen U, Davis EM, Le Beau MM, Stoffel W: Human mitochondrial enoyl-CoA hydratase gene (ECHS1): structural organization and assignment to chromosome 10q26.2-q26.3. Genomics. 1997 Mar 15;40(3):470-5. [PubMed:9073515 ]
  7. Hubbard MJ, McHugh NJ: Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping. Electrophoresis. 2000 Nov;21(17):3785-96. [PubMed:11271497 ]